Biochemistry 4th Edition by Donald Voet – Test Bank

E) cis F) trans G) sterically forbidden conformation H) regular secondary structure I) collagen J) peptide bond K) ribonuclease A (RNase A) L) alpha 1. Repeating values of f and y make up predictable orientations of amino acid with a chain, this predictable orientation forms___________. Ans: H Level of Difficulty: Easy Section 6.1.B Learning objective: Secondary Structure 2. The strength of _______ comes from close packing of glycine residues and the characteristics of hydroxyproline allowing formation of a lefthanded helical conformation which combines with two other left handed structures to form a right-handed triplet helix. Ans: I Level of Difficulty: Easy Section 6.1.C Learning Objective: Secondary Structure 3. The overall arrangement of the regular structural elements such as the α helix and the β sheet in the protein are considered the protein’s ______. Ans: A Level of Difficulty: Easy Section 6.2.C Learning Objective: Tertiary Structure 4. A historical experiment exploring denaturation upon β- mercaptoethanol reduction of disulfide bonds and spontaneous renaturation upon dialysis to remove the β- mercaptoethanol was carried out using the protein ______. This experiment demonstrated the importance of disulfide bonds and amino acid sequence in folding of proteins. Ans: K Level of Difficulty: Easy Section 6.4.B Learning Objective: Protein Stability